1un9: Difference between revisions

Revision as of 02:54, 28 July 2008

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File:1un9.png

Template:STRUCTURE 1un9

CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM C. FREUNDII IN COMPLEX WITH AMP-PNP AND MG2+CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM C. FREUNDII IN COMPLEX WITH AMP-PNP AND MG2+

Template:ABSTRACT PUBMED 12966101

About this StructureAbout this Structure

1UN9 is a Single protein structure of sequence from Citrobacter freundii. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain., Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B, J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. PMID:12966101

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-'''CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM C. FREUNDII IN COMPLEX WITH AMP-PNP AND MG2+'''
+===CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM C. FREUNDII IN COMPLEX WITH AMP-PNP AND MG2+===
-==Overview==
+<!--
-Dihydroxyacetone kinases are a sequence-conserved family of enzymes, which utilize two different phosphoryldonors, ATP in animals, plants and some bacteria, and a multiphosphoprotein of the phosphoenolpyruvate carbohydrate phosphotransferase system in bacteria. Here we report the 2.5-A crystal structure of the homodimeric Citrobacter freundii dihydroxyacetone kinase complex with an ATP analogue and dihydroxyacetone. The N-terminal domain consists of two alpha/beta-folds with a molecule of dihydroxyacetone covalently bound in hemiaminal linkage to the N epsilon 2 of His-220. The C-terminal domain consists of a regular eight-helix alpha-barrel. The eight helices form a deep pocket, which includes a tightly bound phospholipid. Only the lipid headgroup protrudes from the surface. The nucleotide is bound on the top of the barrel across from the entrance to the lipid pocket. The phosphate groups are coordinated by two Mg2+ ions to gamma-carboxyl groups of aspartyl residues. The ATP binding site does not contain positively charged or aromatic groups. Paralogues of dihydroxyacetone kinase also occur in association with transcription regulators and proteins of unknown function pointing to biological roles beyond triose metabolism.
+The line below this paragraph, {{ABSTRACT_PUBMED_12966101}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12966101 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12966101}}
 ==About this Structure==
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 [[Category: Dihydroxyacetone kinase]]
 [[Category: Kinase,glycerone kinase]]
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